Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Dag E. Helland"'
Publikováno v:
FEBS Letters. 484:43-47
Four monoclonal antibodies (MAbs) recognizing HIV-1 reverse transcriptase (RT) were shown here to cross-react with the beta' subunit of Escherichia coli RNA polymerase (RNAP). The anti-RT MAbs bind to a peptide comprising residues 294-305 of the RT a
Publikováno v:
AIDS Research and Human Retroviruses. 12:611-619
In the present study, a CAT assay, a beta-galactosidase assay, and immunofluorescence analysis have been used to study the cellular uptake of the HIV-1 Tat protein. An anti-Tat MAb binding to an epitope comprising both the basic domain and the RGD se
Publikováno v:
Journal of Virology. 70:1580-1587
Human immunodeficiency virus type 1 (HIV-1) integrase (IN) catalyzes the integration of viral DNA into the host chromosome, an essential step in retroviral replication. As a tool to study the structure and function of this enzyme, monoclonal antibodi
Autor:
Magnar Ulstein, Bjørn Haneberg, Roland Jonsson, Inger Lise Haugen, Asbjørn Digranes, Knut Hordnes, Dag E. Helland
Publikováno v:
Journal of Reproductive Immunology. 28:247-262
The cervico-vaginal mucosa is poorly designed for inducing a mucosal immune response, but it can effect such a response evoked at other mucosal sites. This study was undertaken to determine whether colonic-rectal immunization with group B streptococc
Autor:
Blandine Monel, Francesca Di Nunzio, Alan Engelman, Lavanya Krishnan, Mohd Jamal Dar, Dag E. Helland, Ming-Chieh Shun
Publikováno v:
Retrovirology
Retrovirology, BioMed Central, 2009, 6 (1), pp.94. ⟨10.1186/1742-4690-6-94⟩
Retrovirology, Vol 6, Iss 1, p 94 (2009)
Retrovirology, BioMed Central, 2009, 6 (1), pp.94. ⟨10.1186/1742-4690-6-94⟩
Retrovirology, Vol 6, Iss 1, p 94 (2009)
Background The 18 residue tail abutting the SH3 fold that comprises the heart of the C-terminal domain is the only part of HIV-1 integrase yet to be visualized by structural biology. To ascertain the role of the tail region in integrase function and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e65f63a32f92f3948da1498b4a6bb162
https://hdl.handle.net/1956/9269
https://hdl.handle.net/1956/9269
Autor:
William A. Haseltine, Dag E. Helland, Richard D. Cummings, Ali Shilatifard, Jacqueline L. Welles, Roberta K. Merkle
Publikováno v:
Archives of Biochemistry and Biophysics. 290:248-257
The envelope glycoprotein of HIV-I in infected, cultured human T cells is synthesized as a precursor of apparent Mr 160 kDa (gp160) and is cleaved to two glycoproteins, gp120 and gp41, which are the mature envelope glycoproteins in the virus. Neither
Publikováno v:
Nucleic Acids Research. 19:4473-4478
We have previously isolated a cDNA encoding a human uracil-DNA glycosylase which is closely related to the bacterial and yeast enzymes. In vitro expression of this cDNA produced a protein with an apparent molecular weight of 34 K in agreement with th
Autor:
Bjarne Bjorvatn, Dag E. Helland
Publikováno v:
Scandinavian Journal of Infectious Diseases. 22:1-88
Publikováno v:
Scopus-Elsevier
The human immunodeficiency virus type 1 (HIV-1) transactivator (tat) protein produced in one cell activated HIV-1 promoter-directed gene expression in a second cell, provided the cells were in direct contact with one another. This observation suggest
Publikováno v:
Genomics. 7:139-141
Using Southern blot analysis of DNA from a panel of rodent-human somatic cell hybrids with known karyotypes, we have assigned the human uracil-DNA glycosylase gene to chromosome 12.